Aβ(1-42) tetramer and octamer structures reveal edge conductivity pores as a mechanism for membrane damage

Molecular dynamics simulations reveal the importance of amyloid

Aβ-Peptide Production and Conformational Behavior

βPFOAβ(1-42) samples can be enriched in either tetramers or

Frontiers Purinergic signaling via P2X receptors and mechanisms

RCSB PDB - 6RHY: Structure of pore-forming amyloid-beta tetramers

Andres Arango

In vivo induction of membrane damage by β-amyloid peptide

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LinkedIn CovalX 페이지: Aβ(1-42) tetramer and octamer structures

Structure of amyloid β25–35 in lipid environment and cholesterol

Aβ42 purification. (A) SDS-PAGE analysis of SUMO-Aβ42 fusion

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Cholesterol Molecules Alter the Energy Landscape of Small Aβ1–42